HEADER TRANSFERASE, LYASE/DNA 07-MAY-13 4KLE
TITLE DNA POLYMERASE BETA MATCHED REACTANT COMPLEX WITH MG2+, 10 S
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*CP*GP*AP*CP*GP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3';
COMPND 3 CHAIN: T;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*CP*C)-3');
COMPND 7 CHAIN: P;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: 5'-D(P*GP*TP*CP*GP*G)-3';
COMPND 11 CHAIN: D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: DNA POLYMERASE BETA;
COMPND 15 CHAIN: A;
COMPND 16 EC: 2.7.7.7, 4.2.99.-;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES;
SOURCE 5 MOL_ID: 3;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 MOL_ID: 4;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: POLB;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: TAP56;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PWL11
KEYWDS DNA POLYMERASE, TRANSFERASE, LYASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.D.FREUDENTHAL,W.A.BEARD,D.D.SHOCK,S.H.WILSON
REVDAT 3 20-SEP-23 4KLE 1 REMARK LINK
REVDAT 2 15-NOV-17 4KLE 1 REMARK
REVDAT 1 17-JUL-13 4KLE 0
JRNL AUTH B.D.FREUDENTHAL,W.A.BEARD,D.D.SHOCK,S.H.WILSON
JRNL TITL OBSERVING A DNA POLYMERASE CHOOSE RIGHT FROM WRONG.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 154 157 2013
JRNL REFN ISSN 0092-8674
JRNL PMID 23827680
JRNL DOI 10.1016/J.CELL.2013.05.048
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7_650
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 3 NUMBER OF REFLECTIONS : 26673
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2644
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 22.1439 - 5.2357 1.00 1432 157 0.1745 0.2245
REMARK 3 2 5.2357 - 4.1648 0.95 1327 149 0.1379 0.1868
REMARK 3 3 4.1648 - 3.6410 0.96 1365 137 0.1507 0.2011
REMARK 3 4 3.6410 - 3.3093 0.99 1399 137 0.1806 0.2391
REMARK 3 5 3.3093 - 3.0728 0.98 1366 149 0.1941 0.2394
REMARK 3 6 3.0728 - 2.8920 0.95 1313 147 0.2011 0.2811
REMARK 3 7 2.8920 - 2.7474 0.94 1292 154 0.2057 0.2822
REMARK 3 8 2.7474 - 2.6280 0.93 1309 139 0.2135 0.2698
REMARK 3 9 2.6280 - 2.5270 0.92 1279 126 0.2096 0.2475
REMARK 3 10 2.5270 - 2.4399 0.90 1274 140 0.2046 0.2562
REMARK 3 11 2.4399 - 2.3637 0.91 1264 139 0.2023 0.2953
REMARK 3 12 2.3637 - 2.2962 0.90 1196 153 0.2043 0.3084
REMARK 3 13 2.2962 - 2.2358 0.88 1244 134 0.2101 0.2787
REMARK 3 14 2.2358 - 2.1813 0.90 1236 156 0.2131 0.3214
REMARK 3 15 2.1813 - 2.1318 0.90 1236 133 0.2139 0.2956
REMARK 3 16 2.1318 - 2.0865 0.85 1166 133 0.2241 0.2840
REMARK 3 17 2.0865 - 2.0448 0.85 1170 142 0.2314 0.3300
REMARK 3 18 2.0448 - 2.0062 0.79 1101 119 0.2423 0.3214
REMARK 3 19 2.0062 - 1.9700 0.76 1060 100 0.2454 0.3283
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 35.30
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.94850
REMARK 3 B22 (A**2) : -1.65950
REMARK 3 B33 (A**2) : -4.28890
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.015 3499
REMARK 3 ANGLE : 1.164 4886
REMARK 3 CHIRALITY : 0.062 525
REMARK 3 PLANARITY : 0.004 514
REMARK 3 DIHEDRAL : 18.799 1375
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4KLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1000079484.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : VARIMAXHF
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 92
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28965
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.31200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2FMS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM IMIDAZOLE, 350 MM SODIUM
REMARK 280 CHLORIDE, 17% PEG3350, PH 8.0, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.66450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, P, D, A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 3
REMARK 465 ARG A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 PRO A 7
REMARK 465 GLN A 8
REMARK 465 GLU A 9
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 470 VAL A 303 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DC P 10 O3' DC P 11 P -0.087
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC T 5 O4' - C1' - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 DG T 6 O4' - C1' - N9 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DC T 8 O4' - C1' - N1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 DG P 9 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 170 117.32 -161.39
REMARK 500 SER A 171 -8.31 -58.71
REMARK 500 CYS A 178 -153.02 -114.35
REMARK 500 GLN A 207 118.55 -161.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 402 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC P 10 O3'
REMARK 620 2 DC P 10 O3' 22.6
REMARK 620 3 DC P 11 OP1 78.3 61.1
REMARK 620 4 HOH P 102 O 81.9 63.8 71.7
REMARK 620 5 ASP A 190 OD2 150.2 131.2 95.1 68.5
REMARK 620 6 ASP A 192 OD1 94.4 107.9 90.9 162.6 114.8
REMARK 620 7 ASP A 256 OD2 80.1 94.4 154.8 92.6 97.3 103.6
REMARK 620 8 DCP A 401 O2A 79.4 63.7 5.5 77.2 96.8 85.5 158.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DC P 11 OP1
REMARK 620 2 ASP A 190 OD1 87.4
REMARK 620 3 ASP A 192 OD2 86.2 97.2
REMARK 620 4 DCP A 401 O2B 90.6 177.3 84.5
REMARK 620 5 DCP A 401 O2G 91.7 93.0 169.5 85.2
REMARK 620 6 DCP A 401 O2A 5.1 86.9 81.2 91.2 96.8
REMARK 620 7 PPV A 404 O21 95.3 95.1 167.7 83.3 4.0 100.3
REMARK 620 8 PPV A 404 O32 100.0 171.8 86.8 9.6 83.4 100.8 80.9
REMARK 620 9 HOH A 502 O 171.5 95.5 85.6 86.8 96.1 166.8 92.4 77.6
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPV A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4KLD RELATED DB: PDB
REMARK 900 RELATED ID: 4KLF RELATED DB: PDB
REMARK 900 RELATED ID: 4KLG RELATED DB: PDB
REMARK 900 RELATED ID: 4KLH RELATED DB: PDB
REMARK 900 RELATED ID: 4KLI RELATED DB: PDB
REMARK 900 RELATED ID: 4KLJ RELATED DB: PDB
REMARK 900 RELATED ID: 4KLL RELATED DB: PDB
REMARK 900 RELATED ID: 4KLM RELATED DB: PDB
REMARK 900 RELATED ID: 4KLO RELATED DB: PDB
REMARK 900 RELATED ID: 4KLP RELATED DB: PDB
REMARK 900 RELATED ID: 4KLQ RELATED DB: PDB
REMARK 900 RELATED ID: 4KLS RELATED DB: PDB
REMARK 900 RELATED ID: 4KLT RELATED DB: PDB
REMARK 900 RELATED ID: 4KLU RELATED DB: PDB
DBREF 4KLE A 1 335 UNP P06746 DPOLB_HUMAN 1 335
DBREF 4KLE T 1 16 PDB 4KLE 4KLE 1 16
DBREF 4KLE P 1 11 PDB 4KLE 4KLE 1 11
DBREF 4KLE D 1 5 PDB 4KLE 4KLE 1 5
SEQRES 1 T 16 DC DC DG DA DC DG DG DC DG DC DA DT DC
SEQRES 2 T 16 DA DG DC
SEQRES 1 P 11 DG DC DT DG DA DT DG DC DG DC DC
SEQRES 1 D 5 DG DT DC DG DG
SEQRES 1 A 335 MET SER LYS ARG LYS ALA PRO GLN GLU THR LEU ASN GLY
SEQRES 2 A 335 GLY ILE THR ASP MET LEU THR GLU LEU ALA ASN PHE GLU
SEQRES 3 A 335 LYS ASN VAL SER GLN ALA ILE HIS LYS TYR ASN ALA TYR
SEQRES 4 A 335 ARG LYS ALA ALA SER VAL ILE ALA LYS TYR PRO HIS LYS
SEQRES 5 A 335 ILE LYS SER GLY ALA GLU ALA LYS LYS LEU PRO GLY VAL
SEQRES 6 A 335 GLY THR LYS ILE ALA GLU LYS ILE ASP GLU PHE LEU ALA
SEQRES 7 A 335 THR GLY LYS LEU ARG LYS LEU GLU LYS ILE ARG GLN ASP
SEQRES 8 A 335 ASP THR SER SER SER ILE ASN PHE LEU THR ARG VAL SER
SEQRES 9 A 335 GLY ILE GLY PRO SER ALA ALA ARG LYS PHE VAL ASP GLU
SEQRES 10 A 335 GLY ILE LYS THR LEU GLU ASP LEU ARG LYS ASN GLU ASP
SEQRES 11 A 335 LYS LEU ASN HIS HIS GLN ARG ILE GLY LEU LYS TYR PHE
SEQRES 12 A 335 GLY ASP PHE GLU LYS ARG ILE PRO ARG GLU GLU MET LEU
SEQRES 13 A 335 GLN MET GLN ASP ILE VAL LEU ASN GLU VAL LYS LYS VAL
SEQRES 14 A 335 ASP SER GLU TYR ILE ALA THR VAL CYS GLY SER PHE ARG
SEQRES 15 A 335 ARG GLY ALA GLU SER SER GLY ASP MET ASP VAL LEU LEU
SEQRES 16 A 335 THR HIS PRO SER PHE THR SER GLU SER THR LYS GLN PRO
SEQRES 17 A 335 LYS LEU LEU HIS GLN VAL VAL GLU GLN LEU GLN LYS VAL
SEQRES 18 A 335 HIS PHE ILE THR ASP THR LEU SER LYS GLY GLU THR LYS
SEQRES 19 A 335 PHE MET GLY VAL CYS GLN LEU PRO SER LYS ASN ASP GLU
SEQRES 20 A 335 LYS GLU TYR PRO HIS ARG ARG ILE ASP ILE ARG LEU ILE
SEQRES 21 A 335 PRO LYS ASP GLN TYR TYR CYS GLY VAL LEU TYR PHE THR
SEQRES 22 A 335 GLY SER ASP ILE PHE ASN LYS ASN MET ARG ALA HIS ALA
SEQRES 23 A 335 LEU GLU LYS GLY PHE THR ILE ASN GLU TYR THR ILE ARG
SEQRES 24 A 335 PRO LEU GLY VAL THR GLY VAL ALA GLY GLU PRO LEU PRO
SEQRES 25 A 335 VAL ASP SER GLU LYS ASP ILE PHE ASP TYR ILE GLN TRP
SEQRES 26 A 335 LYS TYR ARG GLU PRO LYS ASP ARG SER GLU
HET DCP A 401 28
HET MG A 402 1
HET MG A 403 1
HET PPV A 404 9
HETNAM DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM PPV PYROPHOSPHATE
FORMUL 5 DCP C9 H16 N3 O13 P3
FORMUL 6 MG 2(MG 2+)
FORMUL 8 PPV H4 O7 P2
FORMUL 9 HOH *267(H2 O)
HELIX 1 1 ASN A 12 VAL A 29 1 18
HELIX 2 2 ALA A 32 TYR A 49 1 18
HELIX 3 3 SER A 55 LYS A 61 1 7
HELIX 4 4 GLY A 66 GLY A 80 1 15
HELIX 5 5 LEU A 82 ASP A 91 1 10
HELIX 6 6 ASP A 91 THR A 101 1 11
HELIX 7 7 GLY A 107 GLU A 117 1 11
HELIX 8 8 THR A 121 ASN A 128 1 8
HELIX 9 9 GLU A 129 LEU A 132 5 4
HELIX 10 10 ASN A 133 TYR A 142 1 10
HELIX 11 11 TYR A 142 GLU A 147 1 6
HELIX 12 12 ARG A 152 ASP A 170 1 19
HELIX 13 13 LYS A 209 VAL A 221 1 13
HELIX 14 14 PRO A 261 ASP A 263 5 3
HELIX 15 15 GLN A 264 GLY A 274 1 11
HELIX 16 16 SER A 275 LYS A 289 1 15
HELIX 17 17 SER A 315 ILE A 323 1 9
HELIX 18 18 GLU A 329 ARG A 333 5 5
SHEET 1 A 2 ILE A 150 PRO A 151 0
SHEET 2 A 2 SER A 187 SER A 188 -1 O SER A 188 N ILE A 150
SHEET 1 B 5 ILE A 174 CYS A 178 0
SHEET 2 B 5 MET A 191 THR A 196 -1 O LEU A 194 N THR A 176
SHEET 3 B 5 ARG A 253 LEU A 259 1 O ASP A 256 N VAL A 193
SHEET 4 B 5 LYS A 234 CYS A 239 -1 N CYS A 239 O ARG A 253
SHEET 5 B 5 ILE A 224 LYS A 230 -1 N LEU A 228 O MET A 236
SHEET 1 C 2 PHE A 291 ILE A 293 0
SHEET 2 C 2 ILE A 298 PRO A 300 -1 O ARG A 299 N THR A 292
LINK O3'A DC P 10 MG MG A 402 1555 1555 2.29
LINK O3'B DC P 10 MG MG A 402 1555 1555 2.37
LINK OP1B DC P 11 MG MG A 402 1555 1555 2.39
LINK OP1B DC P 11 MG MG A 403 1555 1555 2.45
LINK O HOH P 102 MG MG A 402 1555 1555 2.11
LINK OD2 ASP A 190 MG MG A 402 1555 1555 2.13
LINK OD1 ASP A 190 MG MG A 403 1555 1555 2.04
LINK OD1 ASP A 192 MG MG A 402 1555 1555 2.13
LINK OD2 ASP A 192 MG MG A 403 1555 1555 2.18
LINK OD2 ASP A 256 MG MG A 402 1555 1555 2.12
LINK O2AADCP A 401 MG MG A 402 1555 1555 2.30
LINK O2BADCP A 401 MG MG A 403 1555 1555 2.13
LINK O2GADCP A 401 MG MG A 403 1555 1555 2.23
LINK O2AADCP A 401 MG MG A 403 1555 1555 2.32
LINK MG MG A 403 O21BPPV A 404 1555 1555 2.20
LINK MG MG A 403 O32BPPV A 404 1555 1555 2.36
LINK MG MG A 403 O HOH A 502 1555 1555 2.07
CISPEP 1 GLY A 274 SER A 275 0 2.36
SITE 1 AC1 21 ARG A 149 GLY A 179 SER A 180 ARG A 183
SITE 2 AC1 21 GLY A 189 ASP A 190 ASP A 192 TYR A 271
SITE 3 AC1 21 THR A 273 GLY A 274 ASP A 276 ASN A 279
SITE 4 AC1 21 MG A 402 MG A 403 HOH A 502 HOH A 504
SITE 5 AC1 21 HOH A 606 DC P 10 HOH P 102 HOH P 107
SITE 6 AC1 21 DG T 6
SITE 1 AC2 8 ASP A 190 ASP A 192 ASP A 256 DCP A 401
SITE 2 AC2 8 MG A 403 DC P 10 DC P 11 HOH P 102
SITE 1 AC3 7 ASP A 190 ASP A 192 DCP A 401 MG A 402
SITE 2 AC3 7 PPV A 404 HOH A 502 DC P 11
SITE 1 AC4 12 ARG A 149 GLY A 179 SER A 180 ARG A 183
SITE 2 AC4 12 SER A 188 GLY A 189 ASP A 190 ASP A 192
SITE 3 AC4 12 MG A 403 HOH A 502 HOH A 504 DC P 11
CRYST1 50.525 79.329 55.146 90.00 107.33 90.00 P 1 21 1 2
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019792 0.000000 0.006176 0.00000
SCALE2 0.000000 0.012606 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018996 0.00000
(ATOM LINES ARE NOT SHOWN.)
END